Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356.
We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence comparisons, the hydrolase activity was predicted to be located at the C terminus. Subsequent cloning and expression of the C-terminal domain in Bacillus subtilis resulted in the functional verification of the enzymatic activity.
Prado Acosta
Mariano
M
Departamento de Química Biológica, Facultad Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina.
Mercedes Palomino
María
M
Allievi
Mariana C
MC
Sanchez Rivas
Carmen
C
Ruzal
Sandra M
SM
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D002473:Cell Wall / Q000378:metabolism; D003001:Cloning, Molecular; D007779:Lactobacillus acidophilus / Q000201:enzymology*; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D016415:Sequence Alignment
D008562:Membrane Glycoproteins; C055764:S-layer proteins; D009238:N-Acetylmuramoyl-L-alanine Amidase